Cell surface antigen CD38 identified as ecto-enzyme of NAD glycohydrolase has hyaluronate-binding activity. 1994

H Nishina, and K Inageda, and K Takahashi, and S Hoshino, and K Ikeda, and T Katada
Department of Life Science, Tokyo Institute of Technology, Yokohama, Japan.

An ecto-enzyme of NAD glycohydrolase induced by retinoic acid in human leukemic HL-60 cells is attributed to the molecule of leukocyte cell surface antigen CD38 (Kontani, K., et al. (1993) J. Biol. Chem. 268, 16895-16898). The cell surface antigen has an amino acid sequence homologous to Aplysia ADP-ribosyl cyclase that catalyzes the conversion of NAD to cyclic ADP-ribose with a calcium-mobilizing activity. A putative hyaluronate (HA)-binding motif which has recently been identified in CD44 antigen existed in the extracellular domain and intracellular amino terminus of CD38 antigen. CD38 antigen was indeed capable of binding to HA in a manner dependent on ionic strength. By contrast, no binding activity was found in Aplysia ADP-ribosyl cyclase. Thus CD38 antigen, like CD44 antigen characterized as a HA-receptor (or binding) protein, may function as an adhesion molecule.

UI MeSH Term Description Entries
D008562 Membrane Glycoproteins Glycoproteins found on the membrane or surface of cells. Cell Surface Glycoproteins,Surface Glycoproteins,Cell Surface Glycoprotein,Membrane Glycoprotein,Surface Glycoprotein,Glycoprotein, Cell Surface,Glycoprotein, Membrane,Glycoprotein, Surface,Glycoproteins, Cell Surface,Glycoproteins, Membrane,Glycoproteins, Surface,Surface Glycoprotein, Cell,Surface Glycoproteins, Cell
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009243 NAD A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed) Coenzyme I,DPN,Diphosphopyridine Nucleotide,Nadide,Nicotinamide-Adenine Dinucleotide,Dihydronicotinamide Adenine Dinucleotide,NADH,Adenine Dinucleotide, Dihydronicotinamide,Dinucleotide, Dihydronicotinamide Adenine,Dinucleotide, Nicotinamide-Adenine,Nicotinamide Adenine Dinucleotide,Nucleotide, Diphosphopyridine
D009244 NAD+ Nucleosidase An enzyme that catalyzes the hydrolysis of nicotinamide adenine dinucleotide (NAD) to NICOTINAMIDE and ADENOSINE DIPHOSPHATE RIBOSE. Some are extracellular (ectoenzymes).The enzyme from some sources also catalyses the hydrolysis of nicotinamide adenine dinucleotide phosphate (NADP). DPNase,Diphosphopyridine Nucleotidase,NAD+ Glycohydrolase,NADase,Diphosphopyridine Nucleotidases,Ecto-NAD+ Glycohydrolase,NAD(P) Nucleosidase,NAD+ Nucleosidases,NAD-Glycohydrolase,NAD-Glycohydrolases,NADP Nucleosidase,NADP-Glycohydrolase,NADases,Ecto NAD+ Glycohydrolase,Glycohydrolase, Ecto-NAD+,Glycohydrolase, NAD+,NAD Glycohydrolase,NAD Glycohydrolases,NADP Glycohydrolase,Nucleosidase, NAD+,Nucleosidase, NADP,Nucleosidases, NAD+,Nucleotidase, Diphosphopyridine,Nucleotidases, Diphosphopyridine
D009699 N-Glycosyl Hydrolases A class of enzymes involved in the hydrolysis of the N-glycosidic bond of nitrogen-linked sugars. Glycoside Hydrolases, Nitrogen-linked,Hydrolases, N-Glycosyl,Nucleosidase,Nucleosidases,Nucleoside Hydrolase,Nitrogen-linked Glycoside Hydrolases,Nucleoside Hydrolases,Glycoside Hydrolases, Nitrogen linked,Hydrolase, Nucleoside,Hydrolases, N Glycosyl,Hydrolases, Nitrogen-linked Glycoside,Hydrolases, Nucleoside,N Glycosyl Hydrolases,Nitrogen linked Glycoside Hydrolases
D002846 Chromatography, Affinity A chromatographic technique that utilizes the ability of biological molecules, often ANTIBODIES, to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Chromatography, Bioaffinity,Immunochromatography,Affinity Chromatography,Bioaffinity Chromatography
D004790 Enzyme Induction An increase in the rate of synthesis of an enzyme due to the presence of an inducer which acts to derepress the gene responsible for enzyme synthesis. Induction, Enzyme
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D006820 Hyaluronic Acid A natural high-viscosity mucopolysaccharide with alternating beta (1-3) glucuronide and beta (1-4) glucosaminidic bonds. It is found in the UMBILICAL CORD, in VITREOUS BODY and in SYNOVIAL FLUID. A high urinary level is found in PROGERIA. Amo Vitrax,Amvisc,Biolon,Etamucine,Healon,Hyaluronan,Hyaluronate Sodium,Hyvisc,Luronit,Sodium Hyaluronate,Acid, Hyaluronic,Hyaluronate, Sodium,Vitrax, Amo
D000246 Adenosine Diphosphate Ribose An ester formed between the aldehydic carbon of RIBOSE and the terminal phosphate of ADENOSINE DIPHOSPHATE. It is produced by the hydrolysis of nicotinamide-adenine dinucleotide (NAD) by a variety of enzymes, some of which transfer an ADP-ribosyl group to target proteins. ADP Ribose,Adenosine Diphosphoribose,ADP-Ribose,ADPribose,Adenosine 5'-Diphosphoribose,5'-Diphosphoribose, Adenosine,Adenosine 5' Diphosphoribose,Diphosphate Ribose, Adenosine,Diphosphoribose, Adenosine,Ribose, ADP,Ribose, Adenosine Diphosphate

Related Publications

H Nishina, and K Inageda, and K Takahashi, and S Hoshino, and K Ikeda, and T Katada
January 2003, Methods in enzymology,
H Nishina, and K Inageda, and K Takahashi, and S Hoshino, and K Ikeda, and T Katada
January 2001, Biochemistry,
H Nishina, and K Inageda, and K Takahashi, and S Hoshino, and K Ikeda, and T Katada
August 1993, The Journal of biological chemistry,
H Nishina, and K Inageda, and K Takahashi, and S Hoshino, and K Ikeda, and T Katada
October 2000, Journal of biochemistry,
H Nishina, and K Inageda, and K Takahashi, and S Hoshino, and K Ikeda, and T Katada
May 1983, The Biochemical journal,
H Nishina, and K Inageda, and K Takahashi, and S Hoshino, and K Ikeda, and T Katada
May 1996, The Journal of biological chemistry,
H Nishina, and K Inageda, and K Takahashi, and S Hoshino, and K Ikeda, and T Katada
November 1998, The Biochemical journal,
H Nishina, and K Inageda, and K Takahashi, and S Hoshino, and K Ikeda, and T Katada
January 2022, mAbs,
H Nishina, and K Inageda, and K Takahashi, and S Hoshino, and K Ikeda, and T Katada
January 2000, The Biochemical journal,
H Nishina, and K Inageda, and K Takahashi, and S Hoshino, and K Ikeda, and T Katada
January 1997, Advances in experimental medicine and biology,
Copied contents to your clipboard!